Sequence of archaeal Methanococcus jannaschii alpha-amylase contains features of families 13 and 57 of glycosyl hydrolases: a trace of their common ancestor?
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
9721603
DOI
10.1007/bf02816496
Knihovny.cz E-resources
- MeSH
- alpha-Amylases chemistry classification MeSH
- Bacillus megaterium enzymology MeSH
- Glycoside Hydrolases chemistry classification MeSH
- Conserved Sequence MeSH
- Methanococcus classification enzymology MeSH
- Molecular Sequence Data MeSH
- Pyrococcus enzymology MeSH
- Amino Acid Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Sequence Alignment MeSH
- Cluster Analysis MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- alpha-Amylases MeSH
- Glycoside Hydrolases MeSH
Two sequentially different, seemingly unrelated alpha-amylase families exist, known as family-13 and family-57 glycosyl hydrolases. Despite the common enzyme activity, it has as yet been impossible to detect any sequence similarity between the two families. The detailed analysis of the recently determined sequence of the alpha-amylase from methanogenic archaeon Methanococcus jannaschii using the sensitive Hydrophobic Cluster Analysis method revealed that this alpha-amylase contains features of both families of alpha-amylases. Thus the M. jannaschii alpha-amylase is similar to the Pyrococcus furiosus alpha-amylase from family 57 while it obviously contains most of the sequence fingerprints characteristic for alpha-amylase family 13. Importantly, a glutamic acid residue equivalent with the family-13 catalytic glutamate positioned in the beta 5-strand segment was identified in members of family 57. The results presented in this report indicate that the two families, 13 and 57, are either the products of a very distant common ancestor or have evolved from each other, although at present they can represent two different alpha-amylase families with evolved different catalytic mechanisms, catalytic machinery and folds.
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Novel, thermostable family-13-like glycoside hydrolase from Methanococcus jannaschii
